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Interleukin 5 receptor alpha subunit

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Title: Interleukin 5 receptor alpha subunit  
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Subject: CXCR6, IL3RA, CCR9, C-C chemokine receptor type 7, CCR8 (gene)
Collection: Clusters of Differentiation
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Interleukin 5 receptor alpha subunit

Interleukin 5 receptor, alpha

Rendering of IL5RA from PDB
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; CD125; CDw125; HSIL5R3; IL5R
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Interleukin 5 receptor, alpha (IL5RA) also known as CD125 (Cluster of Differentiation 125) is a subunit of the Interleukin-5 receptor. IL5RA also denotes its human gene.[1] The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is composed of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Six alternatively spliced transcript variants encoding three distinct isoforms have been reported.[1]

Contents

  • Interactions 1
  • See also 2
  • References 3
  • Further reading 4
  • External links 5

Interactions

Interleukin 5 receptor alpha subunit has been shown to interact with Protein unc-119 homolog,[2] Interleukin 5,[3][4][5] SDCBP[6] and Janus kinase 2.[7]

See also

References

  1. ^ a b "Entrez Gene: IL5RA interleukin 5 receptor, alpha". 
  2. ^ Cen, Osman; Gorska Magdalena M; Stafford Susan J; Sur Sanjiv; Alam Rafeul (Mar 2003). "Identification of UNC119 as a novel activator of SRC-type tyrosine kinases". J. Biol. Chem. (United States) 278 (10): 8837–45.  
  3. ^ Woodcock, J M; Zacharakis B; Plaetinck G; Bagley C J; Qiyu S; Hercus T R; Tavernier J; Lopez A F (Nov 1994). "Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF". EMBO J. (ENGLAND) 13 (21): 5176–85.  
  4. ^ Johanson, K; Appelbaum E; Doyle M; Hensley P; Zhao B; Abdel-Meguid S S; Young P; Cook R; Carr S; Matico R (Apr 1995). "Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins". J. Biol. Chem. (UNITED STATES) 270 (16): 9459–71.  
  5. ^ Murata, Y; Takaki S; Migita M; Kikuchi Y; Tominaga A; Takatsu K (Feb 1992). "Molecular cloning and expression of the human interleukin 5 receptor". J. Exp. Med. (UNITED STATES) 175 (2): 341–51.  
  6. ^ Geijsen, N; Uings I J; Pals C; Armstrong J; McKinnon M; Raaijmakers J A; Lammers J W; Koenderman L; Coffer P J (Aug 2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein".  
  7. ^ Ogata, N; Kouro T; Yamada A; Koike M; Hanai N; Ishikawa T; Takatsu K (Apr 1998). "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation". Blood (UNITED STATES) 91 (7): 2264–71.  

Further reading

  • Isobe M, Kumura Y, Murata Y, et al. (1992). "Localization of the gene encoding the alpha subunit of human interleukin-5 receptor (IL5RA) to chromosome region 3p24-3p26.". Genomics 14 (3): 755–8.  
  • Tuypens T, Plaetinck G, Baker E, et al. (1993). "Organization and chromosomal localization of the human interleukin 5 receptor alpha-chain gene.". Eur. Cytokine Netw. 3 (5): 451–9.  
  • Tavernier J, Tuypens T, Plaetinck G, et al. (1992). "Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit.". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 7041–5.  
  • Scott HS, Guo XH, Hopwood JJ, Morris CP (1992). "Structure and sequence of the human alpha-L-iduronidase gene.". Genomics 13 (4): 1311–3.  
  • Murata Y, Takaki S, Migita M, et al. (1992). "Molecular cloning and expression of the human interleukin 5 receptor.". J. Exp. Med. 175 (2): 341–51.  
  • Tavernier J, Devos R, Cornelis S, et al. (1991). "A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF.". Cell 66 (6): 1175–84.  
  • Johanson K, Appelbaum E, Doyle M, et al. (1995). "Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins.". J. Biol. Chem. 270 (16): 9459–71.  
  • Sun Z, Yergeau DA, Tuypens T, et al. (1995). "Identification and characterization of a functional promoter region in the human eosinophil IL-5 receptor alpha subunit gene.". J. Biol. Chem. 270 (3): 1462–71.  
  • Hori K, Hirashima M, Ueno M, et al. (1993). "Regulation of eosinophil migration by adult T cell leukemia-derived factor.". J. Immunol. 151 (10): 5624–30.  
  • Huston MM, Moore JP, Mettes HJ, et al. (1996). "Human B cells express IL-5 receptor messenger ribonucleic acid and respond to IL-5 with enhanced IgM production after mitogenic stimulation with Moraxella catarrhalis.". J. Immunol. 156 (4): 1392–401.  
  • Monahan J, Siegel N, Keith R, et al. (1997). "Attenuation of IL-5-mediated signal transduction, eosinophil survival, and inflammatory mediator release by a soluble human IL-5 receptor.". J. Immunol. 159 (8): 4024–34.  
  • Ogata N, Kouro T, Yamada A, et al. (1998). "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation.". Blood 91 (7): 2264–71.  
  • Tavernier J, Van der Heyden J, Verhee A, et al. (2000). "Interleukin 5 regulates the isoform expression of its own receptor alpha-subunit.". Blood 95 (5): 1600–7.  
  • Czabotar PE, Holland J, Sanderson CJ (2000). "Identification of regions within the third FnIII-like domain of the IL-5Ralpha involved in IL-5 interaction.". Cytokine 12 (7): 867–73.  
  • Plugariu CG, Wu SJ, Zhang W, Chaiken I (2001). "Multisite mutagenesis of interleukin 5 differentiates sites for receptor recognition and receptor activation.". Biochemistry 39 (48): 14939–49.  
  • Geijsen N, Uings IJ, Pals C, et al. (2001). "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein.". Science 293 (5532): 1136–8.  
  • Upham JW, Sehmi R, Hayes LM, et al. (2002). "Retinoic acid modulates IL-5 receptor expression and selectively inhibits eosinophil-basophil differentiation of hemopoietic progenitor cells.". J. Allergy Clin. Immunol. 109 (2): 307–13.  
  • Rizzo CA, Yang R, Greenfeder S, et al. (2002). "The IL-5 receptor on human bronchus selectively primes for hyperresponsiveness.". J. Allergy Clin. Immunol. 109 (3): 404–9.  
  • Scibek JJ, Evergren E, Zahn S, et al. (2003). "Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL5:IL5R(alpha) complexes.". Anal. Biochem. 307 (2): 258–65.  
  • Liu LY, Sedgwick JB, Bates ME, et al. (2002). "Decreased expression of membrane IL-5 receptor alpha on human eosinophils: I. Loss of membrane IL-5 receptor alpha on airway eosinophils and increased soluble IL-5 receptor alpha in the airway after allergen challenge.". J. Immunol. 169 (11): 6452–8.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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